Oxymedin

Product status information

Chemical reagent intended exclusively for laboratory tests (Research Use Only). It is not a medicinal product, dietary supplement or food. It is not intended for use on humans or animals. Sales only to registered research units and laboratories.

Regulatory status (critical)

Oxymedin is the commercial name of Pro-Body for IGF-1 LR3 (Long R3 IGF-1) — a synthetic analogue of insulin-like growth factor type 1. IGF-1 and its analogues are on the prohibited list WADA category S2 (peptide hormones, growth factors, related substances and mimetics) — as growth factors, they are prohibited permanently (in-competition and out-of-competition). Registered athletes (ADAMS) must absolutely check the current list of prohibited substances before making any decision. Communicating the product as a “massing”, “regeneration”, “anabolic” or “muscle growth” product in humans is contrary to the Research Use Only framework.

Oxymedin from the line Endogenic is a reagent that reproduces one of the best-characterized modified analogues of the body’s signaling molecule – insulin-like growth factor type 1 (IGF-1). Under the trade name Oxymedin Pro-Body, it provides exactly the compound that in the literature functions as IGF-1 LR3 (Long R3 IGF-1): a synthetic, extended variant of native IGF-1, designed to act longer and to a greater extent as a free peptide available to the receptor.

The Endogenic line includes Pro-Body reagents focused on enzymes, hormones and endogenous metabolism signals – the same family of research tools from the category HGH and IGF-1 LR3, which includes recombinant growth hormone Oxytropin with bacteriostatic water and GH secretary MK-677. Oxymedin fits into it as a tool for examining the final link of the GH-IGF-1 axis: it is not a secretagogue that releases growth hormone or the growth hormone itself, but an analogue of the effector of this axis – a factor that mediates a significant part of the anabolic effects of GH at the tissue level.

This reagent is supplied as a vial of lyophilisate (dry powder) for self-reconstitution — a format that gives the researcher the freedom to select the working concentration for a specific experimental setup. Purity verified by HPLC ≥98%, identity confirmed by Q-TOF mass spectrometry, COA available for each batch. It is a molecular tool for research on IGF-1 receptor signaling, muscle anabolism, cell proliferation and tissue regeneration – exclusively in laboratory conditions.

Insulin-like growth factor type 1 (IGF-1) is an endogenous peptide with a structure similar to proinsulin, produced mainly in the liver under the control of growth hormone (GH). The GH–IGF-1 axis operates in a cascade: the hypothalamus and pituitary regulate GH secretion, GH stimulates the liver and peripheral tissues to produce IGF-1, and IGF-1 is the actual effector translating the signal into cell proliferation, differentiation and growth.

A significant part of the anabolic effect of GH is carried out by IGF-1. Native IGF-1 almost never circulates as a free peptide in the bloodstream. It is bound by a family of six insulin-like growth factor binding proteins (IGFBPs), which regulate its stability, half-life and receptor availability. IGFBPs act as a reservoir and gate: on the one hand, they prolong the presence of IGF-1 in the circulation, and on the other, they limit the pool of peptide capable of immediately stimulating the receptor.

This affinity for IGFBP is the central point around which IGF-1 analogues are designed. The world of metabolism, muscle and recovery research is watching IGF-1 and its analogues for several reasons. First, IGF-1 acts through IGF-1 receptor (IGF-1R) — a receptor with tyrosine kinase activity, triggering the PI3K/Akt and MAPK cascades, central to protein synthesis, cell survival and proliferation.

Secondly, structural modifications (Arg in position 3, extension of the N-terminus) allow to change the affinity for IGFBP to obtain a longer-acting, more available peptide – this is the essence of IGF-1 LR3 delivered as Oxymedin. Third, the IGF-1 axis is in the field of research on muscle hyperplasia, tissue regeneration and glucose metabolism.

Chemically, Oxymedin is IGF-1 LR3 (Long R3 IGF-1) — 83-amino acid analogue of human IGF-1. It is created from the native, 70-amino-acid IGF-1 sequence by two coupled modifications that together give the molecule its characteristic profile.

• Substitution at position 3 — native glutamic acid (Glu) was replaced by arginine (Arg). This is the root of the designation “R3” (Arg³).
• N-terminal extension — an additional fragment of 13 amino acids has been added to the N-terminus, which prolongs the action of the molecule. This is the root of the “Long” (L) designation.

Together they give a chain of 83 amino acid residues. The meaning of both changes is one: significantly reduce the affinity of the analogue for IGF-binding proteins (IGFBPs). Less binding by IGFBP means a much longer half-life and a larger pool of free, receptor-available peptide compared to native IGF-1.

• Trade name Pro-Body: Oxymedin
• Name in the literature: IGF-1 LR3 (Long R3 IGF-1)
• Class: insulin-like growth factor type 1 analogue; IGF-1R receptor agonist
• Number of amino acids: 83 (native IGF-1: 70 aa + N-terminal extension 13 aa)
• Modifications: Arg instead of Glu at position 3 (Arg³) + extension of the N-terminus by 13 amino acids
• CAS number: 946870-92-4 — for verification in the batch COA
• Molecular weight: ~9111 g/mol — for verification in the batch COA
• Molecular target/axis: IGF-1 receptor (IGF-1R); PI3K/Akt and MAPK cascades; GH–IGF-1 axis
• Delivered form: vial of lyophilisate (dry powder) for reconstitution; ≥98% HPLC

Characteristics table

In the literature, IGF-1 LR3 is described as a growth factor analogue acting through the IGF-1 receptor, the stimulation of which triggers anabolic and proliferative cascades. The literature points to five related axes observed in the models. Below, each with the name of the pathway and its translation into experimental observations – all relating to molecular biology and research models, not applicable to humans.

IGF-1R receptor agonism – PI3K/Akt and MAPK cascades

Central mechanism. IGF-1 LR3 binds to IGF-1 receptor (IGF-1R) — a receptor with tyrosine kinase activity. Stimulation of the receptor autophosphorylates its intracellular domains and triggers two main cascades: PI3K/Akt (central for protein synthesis, cell survival and glucose metabolism) and MAPK (related to proliferation and differentiation). This is the molecular core of the profile for which the analogue is being explored as an anabolic and proliferative signaling tool.

LR3 modification and affinity for IGFBP – prolonged action

The second axis concerns pharmacokinetics and is the defining feature of the analogue. Arg³ substitution and N-terminal extension significantly reduce the affinity of the molecule for IGF-binding proteins (IGFBPs). Native IGF-1 is largely taken up by IGFBP, which limits the pool of free peptide and modulates its half-life. IGF-1 LR3, bound by IGFBPs significantly weaker, circulates longer and remains available to the IGF-1R receptor to a greater extent. In models, this translates into longer and more pronounced receptor stimulation compared to native IGF-1.

Anabolism – muscle protein synthesis

The third axis includes muscle anabolism. Through the PI3K/Akt cascade, IGF-1R activation enhances muscle protein synthesis and inhibits their degradation pathways. In cellular and animal models, IGF-1 and its analogues have been associated with a positive protein balance in muscle tissue (Tomas et al. 1992; Adams 2002). This is the direction that drives research on anabolism and muscle hypertrophy.

Hyperplasia – proliferation of myoblasts and satellite cells

The fourth axis concerns cell proliferation. Through the MAPK cascade and proliferative signaling, IGF-1 stimulates in models proliferation of myoblasts and satellite cells — a mechanism related to hyperplasia (an increase in the number of cells), different from the mere hypertrophy of existing fibers. In research on muscle regeneration and growth, IGF-1 is described as a factor supporting the activation and proliferation of satellite cells (Philippou and Barton 2014).

Hypoglycemic effect – affinity for the insulin receptor

The fifth axis results from the structural similarity of IGF-1 to insulin. IGF-1 and its analogues show some affinity for the insulin receptor, which translates into the effect in the models hypoglycemic (lowering glucose levels). Due to the prolonged effect and greater availability of free peptide, this effect is sometimes indicated in the literature as an important parameter of the IGF-1 LR3 profile.

This is an observation from molecular biology and models, not a declaration of effect in humans. In addition to these five axes, IGF-1 is widely studied in context in the literature tissue regeneration and growth (Clemmons 2012; Yakar and Adamo 2012) – from muscles through bone tissue to other proliferating tissues. Reference data mainly comes from work on the biology of IGF-1 and the GH–IGF-1 axis and on the anabolic profile of analogues (Tomas et al. 1992; Adams 2002).

IMPORTANT DISTINCTION

“Has an anabolic effect” or “stimulates protein synthesis” in the context of this description means: “in vitro and in vivo studies in animal models have observed the effect of IGF-1 LR3 on the IGF-1R receptor, PI3K/Akt and MAPK cascades, and markers of protein synthesis and cell proliferation.” This is not a guarantee of effect in humans or a suggestion that the Oxymedin reagent may function as an anabolic, mass-building or regenerative agent in humans.

Four distinctions are also necessary. Oxymedin is the trade name of IGF-1 LR3 — the same compound, only the trade name, not the molecule, differs. IGF-1 LR3 vs IGF-1 DES vs native IGF-1. IGF-1 LR3 (longer half-life, significantly lower IGFBP binding) differs from the analogue with high local potency IGF-1 DES, i.e. the des(1-3) variant with the first three N-terminal residues removed, higher local potency and short half-life; both differ from native, 70-amino acid IGF-1.

IGF-1 LR3 acts through IGF-1R, not the GH receptor. This is a different starting point than recombinant growth hormone, which works through the GH receptor (GHR) higher in the axis. All mechanisms described refer only to observations in preclinical models.

Oxymedin (IGF-1 LR3) as an RUO reagent is used as a molecular tool in research on IGF-1 receptor signaling and the biology of anabolism. In vitro models (cultures of myoblasts, satellite cells, cell lines expressing IGF-1R) examine its effect on receptor activation, PI3K/Akt and MAPK cascades, protein synthesis and cell proliferation. In vivo animal models analyze the impact on muscle tissue anabolism, regeneration and glucose metabolism parameters. Among the tools from the group peptides for muscle mass IGF-1 analogues are among the most frequently studied models of anabolic signaling. Specific research directions include:

• IGF-1R receptor signaling — studies of PI3K/Akt and MAPK cascades, binding kinetics and signal specificity in cell cultures expressing the receptor
• Muscle anabolism and protein synthesis — cellular and animal models, measurements of protein balance and synthesis markers (Tomas et al. 1992; Adams 2002)
• Hyperplasia and satellite cells — proliferation of myoblasts and satellite cells as a mechanism of cell number increase (Philippou and Barton 2014)
• The role of IGFBP in peptide availability — comparison of the LR3 analogue with native IGF-1 in terms of affinity for binding proteins and half-life (Clemmons 2012)
• Tissue regeneration and growth — IGF-1 as a growth factor in models of muscle, bone and other proliferating tissue regeneration (Yakar and Adamo 2012)

Oxymedin (lyophilisate vial, Endogenic line) is the trade name of Pro-Body for IGF-1 LR3 (Long R3 IGF-1) — an 83-amino-acid analogue of insulin-like growth factor type 1. It is created from the native, 70-amino-acid IGF-1 by substituting arginine at position 3 (Arg³) and extending the N-terminus by 13 amino acids. Both modifications clearly reduce the affinity for IGF-binding proteins (IGFBPs), thanks to which the analogue circulates longer and remains more available to the receptor than native IGF-1.

It acts through IGF-1 receptor (IGF-1R) — PI3K/Akt and MAPK cascades — in models associated with muscle protein synthesis, hyperplasia (proliferation of myoblasts and satellite cells), hypoglycemic effect (affinity for the insulin receptor) and tissue regeneration and growth (Clemmons 2012; Yakar and Adamo 2012). Oxymedin = IGF-1 LR3 — the same compound as the generic variant; differs from IGF-1 DES (des(1-3), higher local potency, short half-life) and from native IGF-1, and acts through IGF-1R, not through the GH receptor (unlike recombinant growth hormone).

Regulatory Status – Research Use Only; no registration; WADA category S2 (growth factors), prohibited. The broader context of the use of IGF-1 and growth hormone analogues in mass building is discussed in the review peptides in bodybuilding.

1. Tomas FM, Knowles SE, Owens PC, Chandler CS, Francis GL, et al. (1992). Insulin-like growth factor-I (IGF-I) and especially IGF-I variants are anabolic in dexamethasone-treated rats. PubMed
2. Clemmons, D. R. (2012). Metabolic actions of insulin-like growth factor-I in normal physiology and diabetes. PubMed
3. Yakar S, Adamo ML (2012). Insulin-like growth factor 1 physiology: lessons from mouse models. PubMed
4. Philippou A, Barton ER (2014). Optimizing IGF-I for skeletal muscle therapeutics. PubMed
5. Adams, G. R. (2002). Invited Review: Autocrine/paracrine IGF-I and skeletal muscle adaptation. PubMed

Chemical reagent Research Use Only. Oxymedin (IGF-1 LR3, lyophilized vial, Endogenic line) in the Pro-Body catalog is not a medicinal product, dietary supplement or food. It is not intended for administration to humans or animals outside a controlled experimental environment. Oxymedin (IGF-1 LR3) is not registered as a medicine in the EU or the USA, and IGF-1 and its analogues are on the WADA prohibited list in the category S2 (growth factors) — permanently prohibited (in- and out-of-competition).

Registered Athletes (ADAMS) must check the current list before making any decision. The information in the description is of an educational and scientific nature and refers to the biology of the molecule and the results reported in the preclinical literature – it does not constitute medical advice or administration instructions.